1ac5

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[[Image:1ac5.png|left|200px]]
 
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==CRYSTAL STRUCTURE OF KEX1(DELTA)P, A PROHORMONE-PROCESSING CARBOXYPEPTIDASE FROM SACCHAROMYCES CEREVISIAE==
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The line below this paragraph, containing "STRUCTURE_1ac5", creates the "Structure Box" on the page.
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<StructureSection load='1ac5' size='340' side='right'caption='[[1ac5]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ac5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AC5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AC5 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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{{STRUCTURE_1ac5| PDB=1ac5 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ac5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ac5 OCA], [https://pdbe.org/1ac5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ac5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ac5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ac5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KEX1_YEAST KEX1_YEAST] Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from the precursors of K1, K2 and K28 killer toxins and a-factor (mating pheromone). Involved in the programmed cell death caused by defective N-glycosylation and contributes also to the active cell death program induced by acetic acid stress or during chronological aging. Promotes cell fusion by proteolytically processing substrates that act in parallel to PRM1 as an alternative fusion machine, as cell wall components, or both.<ref>PMID:3301004</ref> <ref>PMID:4364866</ref> <ref>PMID:773743</ref> <ref>PMID:3305079</ref> <ref>PMID:3301840</ref> <ref>PMID:1469044</ref> <ref>PMID:8416959</ref> <ref>PMID:10972812</ref> <ref>PMID:11988505</ref> <ref>PMID:17210951</ref> <ref>PMID:18474590</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ac/1ac5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ac5 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Kex1p is a prohormone-processing serine carboxypeptidase found in Saccharomyces cerevisiae. In contrast to yeast serine carboxypeptidase (CPD-Y) and wheat serine carboxypeptidase II (CPDW-II), Kex1p displays a very narrow specificity for lysyl or arginyl residues at the C-terminus of the substrate. The structure of Kex1Deltap, an enzyme that lacks the acidic domain and membrane-spanning portion of Kex1p, has been solved by a combination of molecular replacement and multiple isomorphous replacement and refined to a resolution of 2.4 A. The S1' site of Kex1Deltap is sterically restricted compared to those from CPD-Y or CPDW-II; it also contains two acidic groups that are well positioned to interact with the basic group of a lysine or arginine side chain. The high specificity of Kex1p can therefore be explained by a combination of steric and electronic factors. The structure of the S1 site of Kex1Deltap is also well suited for binding of a lysine or arginine side chain, and the enzyme may therefore exhibit a preference for these residues at P1.
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===CRYSTAL STRUCTURE OF KEX1(DELTA)P, A PROHORMONE-PROCESSING CARBOXYPEPTIDASE FROM SACCHAROMYCES CEREVISIAE===
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Crystal structure of Kex1deltap, a prohormone-processing carboxypeptidase from Saccharomyces cerevisiae,.,Shilton BH, Thomas DY, Cygler M Biochemistry. 1997 Jul 22;36(29):9002-12. PMID:9220988<ref>PMID:9220988</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_8745419}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1ac5" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 8745419 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_8745419}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1AC5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AC5 OCA].
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==Reference==
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Crystallization of a soluble form of the Kex1p serine carboxypeptidase from Saccharomyces cerevisiae., Shilton BH, Li Y, Tessier D, Thomas DY, Cygler M, Protein Sci. 1996 Feb;5(2):395-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8745419 8745419]
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[[Category: Carboxypeptidase D]]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Cygler M]]
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[[Category: Cygler, M.]]
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[[Category: Shilton BH]]
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[[Category: Shilton, B H.]]
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[[Category: Thomas DY]]
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[[Category: Thomas, D Y.]]
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[[Category: Carboxypeptidase]]
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[[Category: Glycoprotein]]
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[[Category: Hydrolase]]
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[[Category: Transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:33:42 2008''
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Current revision

CRYSTAL STRUCTURE OF KEX1(DELTA)P, A PROHORMONE-PROCESSING CARBOXYPEPTIDASE FROM SACCHAROMYCES CEREVISIAE

PDB ID 1ac5

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